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Database: UniProt
Entry: A0A0F4YW43_TALEM
LinkDB: A0A0F4YW43_TALEM
Original site: A0A0F4YW43_TALEM 
ID   A0A0F4YW43_TALEM        Unreviewed;       605 AA.
AC   A0A0F4YW43;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN   ORFNames=T310_3435 {ECO:0000313|EMBL:KKA22522.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22522.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA22522.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22522.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       {ECO:0000256|ARBA:ARBA00002169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000960,
CC         ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKA22522.1}.
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DR   EMBL; LASV01000138; KKA22522.1; -; Genomic_DNA.
DR   RefSeq; XP_013329134.1; XM_013473680.1.
DR   AlphaFoldDB; A0A0F4YW43; -.
DR   STRING; 1408163.A0A0F4YW43; -.
DR   GeneID; 25315784; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 2.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU00555};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           21..605
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005117066"
FT   DOMAIN          40..571
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   605 AA;  66993 MW;  C7CD224F8483053D CRC64;
     MMRWIAVSGL IVTLAAYGEC YNSTAVEQQL AESYAPITVA CPSDVEWIRP ATGLNPKERD
     WVYGRKKTVL FALGDYLDRL DMQDFDVGEY ICRLRENDYV HVPTIGFAIS GGGWASALTG
     TGALRALDSL EAAREQGTGG LLQSMTYISG LSGGGWPVMS FAAHNFPTAD EILVRWQPQI
     SRLFAQNNSQ YAATGESMFE DLAAKAQAGF NVSVADYMSR AWSYEFVPGP HGGLNVTLSS
     IAKLSNFVNH QMPMPLFQAP FVVDQDVEYY GIKVPFKNIR IHAVRVRQLG RVHASIHPDG
     MAGDCPGPGI RRKRERVHLI EPAKIIIIIN DIVPRGGLPR GRHRSAGLRI HATFRESLSQ
     ISYAWYPNPF ADLASVSSDI RYSSSLRLVD GSENGQASPL WTQIQPARNS SFIIAWDDNT
     DAPPYFWNNG TNLYNTYLRA NETGIPFPIV PSASTFIARN YTTRPVFFGC DANLTTTRDA
     RAPIVAYFAN ASYSAYTNMT FIQTNTSFAQ VREIWVNSFN QMTQANGTLD GEWPVCLGCA
     AIEGSLAKVG LRRTEQCQRC FDRYCWDGVA VEEQPGTEVV DPSLVLDPEL GFLEWVKTNP
     FGTKK
//
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